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从产色沙雷氏菌 UTAD54 中分离到的 B2 型金属β-内酰胺酶 Sfh-I 的生化特性研究

Biochemical characterization of Sfh-I, a subclass B2 metallo-beta-lactamase from Serratia fonticola UTAD54.

机构信息

CESAM & Department of Biology, University of Aveiro, 3810-193 Aveiro, Portugal.

出版信息

Antimicrob Agents Chemother. 2011 Nov;55(11):5392-5. doi: 10.1128/AAC.00429-11. Epub 2011 Aug 29.

DOI:10.1128/AAC.00429-11
PMID:21876065
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3195014/
Abstract

The subclass B2 metallo-β-lactamase (MBL) Sfh-I from Serratia fonticola UTAD54 was cloned and overexpressed in Escherichia coli. The recombinant protein binds one equivalent of zinc, as shown by mass spectrometry, and preferentially hydrolyzes carbapenem substrates. However, compared to other B2 MBLs, Sfh-I also shows limited hydrolytic activity against some additional substrates and is not inhibited by a second equivalent of zinc. These data confirm Sfh-I to be a subclass B2 metallo-β-lactamase with some distinctive properties.

摘要

从粘质沙雷氏菌 UTAD54 中克隆并在大肠杆菌中过表达了子类 B2 金属β-内酰胺酶 (MBL) Sfh-I。质谱分析表明，重组蛋白结合一个当量的锌，并且优先水解碳青霉烯类底物。然而，与其他 B2 MBL 相比，Sfh-I 对一些额外的底物的水解活性也有限，并且不受第二个当量锌的抑制。这些数据证实 Sfh-I 为具有一些独特性质的子类 B2 金属β-内酰胺酶。

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本文引用的文献

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J Mol Biol. 2011 Sep 2;411(5):951-9. doi: 10.1016/j.jmb.2011.06.043. Epub 2011 Jul 6.
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Emerging carbapenemases: a global perspective.新兴碳青霉烯酶：全球视角。
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The structure of the dizinc subclass B2 metallo-beta-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site.双锌B2类金属β-内酰胺酶CphA的结构表明，第二个抑制性锌离子结合在组氨酸位点。
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